2q5d | pdb_00002q5d

Crystal Structure of Human Importin Beta bound to the Snurportin1 IBB-domain second crystal form

spinqualitylabelsall models 2q5d, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2q5d is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2p8q, 1qgk, 1ukl Gene: KPNB1, NTF97 (HUMAN) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The nuclear import of uridine-rich ribonucleoproteins is mediated by the transport adaptor snurportin 1 (SNP1). Similar to importin alpha, SNP1 uses an N-terminal importin beta binding (sIBB) domain to recruit the receptor importin beta and gain access to the nucleus. In this study, we demonstrate that the sIBB domain has a bipartite nature, which contains two distinct binding determinants for importin beta. The first determinant spans residues 25-65 and includes the previously identified importin alpha IBB (alphaIBB) region of homology. The second binding determinant encompasses residues 1-24 and resembles region 1011-1035 of the nucleoporin 153 (Nup153). The two binding determinants synergize within the sIBB domain to confer a low nanomolar binding affinity for importin beta (K(d) approximately 2 nm) in an interaction that, in vitro, is displaced by RanGTP. We propose that in vivo the synergy of Nup153 and nuclear RanGTP promotes translocation of uridine-rich ribonucleoproteins into the nucleus. Molecular basis for the recognition of snurportin 1 by importin beta.,Mitrousis G, Olia AS, Walker-Kopp N, Cingolani G J Biol Chem. 2008 Mar 21;283(12):7877-84. Epub 2008 Jan 9. PMID:18187419 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Importin

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